ZFIN ID: ZDB-PUB-131105-14
The BTB-Containing Protein Kctd15 Is SUMOylated In Vivo
Zarelli, V.E., and Dawid, I.B.
Date: 2013
Source: PLoS One   8(9): e75016 (Journal)
Registered Authors: Dawid, Igor B., Zarelli, Valeria
Keywords: none
MeSH Terms:
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • HEK293 Cells
  • Humans
  • Molecular Sequence Data
  • Mutant Proteins/metabolism
  • Neural Crest/metabolism
  • Potassium Channels/chemistry
  • Potassium Channels/metabolism*
  • Potassium Channels, Voltage-Gated/chemistry
  • Potassium Channels, Voltage-Gated/metabolism*
  • Protein Binding
  • Protein Transport
  • Recombinant Fusion Proteins/metabolism
  • SUMO-1 Protein/metabolism
  • Subcellular Fractions/metabolism
  • Substrate Specificity
  • Sumoylation*
  • Transcription Factor AP-2/metabolism
  • Zebrafish/metabolism
  • Zebrafish Proteins/chemistry
  • Zebrafish Proteins/metabolism*
PubMed: 24086424 Full text @ PLoS One
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ABSTRACT

Potassium Channel Tetramerization Domain containing 15 (Kctd15) has a role in regulating the neural crest (NC) domain in the embryo. Kctd15 inhibits NC induction by antagonizing Wnt signaling and by interaction with the transcription factor AP-2α activation domain blocking its activity. Here we demonstrate that Kctd15 is SUMOylated by SUMO1 and SUMO2/3. Kctd15 contains a classical SUMO interacting motif, ωKxE, at the C-terminal end, and variants of the motif within the molecule. Kctd15 SUMOylation occurs exclusively in the C-terminal motif. Inability to be SUMOylated did not affect Kctd15's subcellular localization, or its ability to repress AP-2 transcriptional activity and to inhibit NC formation in zebrafish embryos. In contrast, a fusion of Kctd15 and SUMO had little effectiveness in AP-2 inhibition and in blocking of NC formation. These data suggest that the non-SUMOylated form of Kctd15 functions in NC development.

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